The formation of electrostatic complexes between beta-casein and iota-and kappa-carrageenans is well-known. However, the molecular mechanism of the complexation has yet to be determined, particularly with respect to the conformational changes of the interacting macromolecules. High-sensitivity differential scanning calorimetry was used to study beta-casein/carrageenan mixtures at different pH values (3.0 to 7.5), ionic strengths (0.03 and 0.15 M), and various molar protein/polysaccharide ratios (3-400). The effects of these variables on the temperature, enthalpy, and width of the helix-coil transition of iota- and kappa-carrageenans were investigated. Neither pH nor the protein/polysaccharide ratio influenced the transition temperature of either carrageenan in the complexes. However, the transition enthalpy of both carrageenans in complexes with beta-casein decreased to zero with both decreasing pH and increasing protein/polysaccharide ratio. This may reflect an unwinding of the polysaccharide double helix induced by beta-casein, a conformational change which is fully reversible in conditions of sufficiently high ionic strength. The interaction of beta-casein with iota- and kappa-carrageenans was approximated in terms of the model of binding of large ligands to macromolecules, that provides the binding constants for these biopolymers.